VASH2_HUMAN
ID VASH2_HUMAN Reviewed; 355 AA.
AC Q86V25; B4DYZ5; Q2VT46; Q5VTE7; Q5VTE9; Q7Z6E3; Q8IZ24; Q9H9W5;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Tubulinyl-Tyr carboxypeptidase 2 {ECO:0000305};
DE EC=3.4.17.17 {ECO:0000269|PubMed:29146869, ECO:0000269|PubMed:31235911};
DE AltName: Full=Vasohibin-2 {ECO:0000303|PubMed:16528006};
DE AltName: Full=Vasohibin-like protein;
GN Name=VASH2 {ECO:0000312|HGNC:HGNC:25723}; Synonyms=VASHL;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=16528006; DOI=10.1161/01.atv.0000216747.66660.26;
RA Shibuya T., Watanabe K., Yamashita H., Shimizu K., Miyashita H., Abe M.,
RA Moriya T., Ohta H., Sonoda H., Shimosegawa T., Tabayashi K., Sato Y.;
RT "Isolation and characterization of vasohibin-2 as a homologue of VEGF-
RT inducible endothelium-derived angiogenesis inhibitor vasohibin.";
RL Arterioscler. Thromb. Vasc. Biol. 26:1051-1057(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 6).
RC TISSUE=Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3; 4 AND 5).
RC TISSUE=Brain, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19204325; DOI=10.1182/blood-2008-07-170316;
RA Kimura H., Miyashita H., Suzuki Y., Kobayashi M., Watanabe K., Sonoda H.,
RA Ohta H., Fujiwara T., Shimosegawa T., Sato Y.;
RT "Distinctive localization and opposed roles of vasohibin-1 and vasohibin-2
RT in the regulation of angiogenesis.";
RL Blood 113:4810-4818(2009).
RN [6]
RP INTERACTION WITH SVBP, AND SUBCELLULAR LOCATION.
RX PubMed=20736312; DOI=10.1242/jcs.067538;
RA Suzuki Y., Kobayashi M., Miyashita H., Ohta H., Sonoda H., Sato Y.;
RT "Isolation of a small vasohibin-binding protein (SVBP) and its role in
RT vasohibin secretion.";
RL J. Cell Sci. 123:3094-3101(2010).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-302, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [8]
RP IDENTIFICATION AS A PROTEASE, AND ACTIVE SITES.
RX PubMed=26794318; DOI=10.1093/bioinformatics/btv761;
RA Sanchez-Pulido L., Ponting C.P.;
RT "Vasohibins: new transglutaminase-like cysteine proteases possessing a non-
RT canonical Cys-His-Ser catalytic triad.";
RL Bioinformatics 32:1441-1445(2016).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH SVBP, ACTIVE SITE, AND
RP MUTAGENESIS OF CYS-158.
RX PubMed=29146869; DOI=10.1126/science.aao5676;
RA Nieuwenhuis J., Adamopoulos A., Bleijerveld O.B., Mazouzi A., Stickel E.,
RA Celie P., Altelaar M., Knipscheer P., Perrakis A., Blomen V.A.,
RA Brummelkamp T.R.;
RT "Vasohibins encode tubulin detyrosinating activity.";
RL Science 358:1453-1456(2017).
RN [10]
RP FUNCTION.
RX PubMed=31171830; DOI=10.1038/s41422-019-0187-y;
RA Liao S., Rajendraprasad G., Wang N., Eibes S., Gao J., Yu H., Wu G., Tu X.,
RA Huang H., Barisic M., Xu C.;
RT "Molecular basis of vasohibins-mediated detyrosination and its impact on
RT spindle function and mitosis.";
RL Cell Res. 29:533-547(2019).
RN [11]
RP INTERACTION WITH SVBP.
RX PubMed=31324789; DOI=10.1038/s41467-019-11277-8;
RA Zhou C., Yan L., Zhang W.H., Liu Z.;
RT "Structural basis of tubulin detyrosination by VASH2/SVBP heterodimer.";
RL Nat. Commun. 10:3212-3212(2019).
RN [12] {ECO:0007744|PDB:6QBY}
RP X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) OF 48-292 IN COMPLEX WITH SVBP AND
RP TUBULIN PEPTIDE, INTERACTION WITH SVBP, FUNCTION, CATALYTIC ACTIVITY,
RP MUTAGENESIS OF 63-TRP--TRP-67; TYR-123; ARG-134; LYS-135; 154-LEU-PRO-155;
RP LYS-157; CYS-158; HIS-192; HIS-193; SER-210; ARG-211 AND LEU-215, AND
RP SUBCELLULAR LOCATION.
RX PubMed=31235911; DOI=10.1038/s41594-019-0241-y;
RA Wang N., Bosc C., Ryul Choi S., Boulan B., Peris L., Olieric N., Bao H.,
RA Krichen F., Chen L., Andrieux A., Olieric V., Moutin M.J., Steinmetz M.O.,
RA Huang H.;
RT "Structural basis of tubulin detyrosination by the vasohibin-SVBP enzyme
RT complex.";
RL Nat. Struct. Mol. Biol. 26:571-582(2019).
CC -!- FUNCTION: Tyrosine carboxypeptidase that removes the C-terminal
CC tyrosine residue of alpha-tubulin, thereby regulating microtubule
CC dynamics and function (PubMed:29146869). Critical for spindle function
CC and accurate chromosome segregation during mitosis since microtuble
CC detyronisation regulates mitotic spindle length and postioning
CC (PubMed:31171830). Acts as an activator of angiogenesis: expressed in
CC infiltrating mononuclear cells in the sprouting front to promote
CC angiogenesis (PubMed:19204325). Plays a role in axon formation
CC (PubMed:31235911). {ECO:0000269|PubMed:19204325,
CC ECO:0000269|PubMed:29146869, ECO:0000269|PubMed:31235911}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=C-terminal L-alpha-aminoacyl-L-glutamyl-L-glutamyl-L-tyrosyl-
CC [tubulin] + H2O = C-terminal L-alpha-aminoacyl-L-glutamyl-L-glutamyl-
CC [tubulin] + L-tyrosine; Xref=Rhea:RHEA:57444, Rhea:RHEA-COMP:16434,
CC Rhea:RHEA-COMP:16435, ChEBI:CHEBI:15377, ChEBI:CHEBI:58315,
CC ChEBI:CHEBI:149554, ChEBI:CHEBI:149555; EC=3.4.17.17;
CC Evidence={ECO:0000269|PubMed:29146869, ECO:0000269|PubMed:31235911};
CC -!- SUBUNIT: Interacts with SVBP; interaction enhances VASH2 tyrosine
CC carboxypeptidase activity. {ECO:0000269|PubMed:20736312,
CC ECO:0000269|PubMed:29146869, ECO:0000269|PubMed:31324789}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19204325}. Secreted
CC {ECO:0000269|PubMed:20736312}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:31235911}. Note=Mainly localizes in the cytoplasm
CC (PubMed:19204325). Some fraction is secreted via a non-canonical
CC secretion system; interaction with SVBP promotes secretion
CC (PubMed:20736312). Associates with microtubules (PubMed:31235911).
CC {ECO:0000269|PubMed:19204325, ECO:0000269|PubMed:20736312,
CC ECO:0000269|PubMed:31235911}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q86V25-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86V25-2; Sequence=VSP_013328;
CC Name=3;
CC IsoId=Q86V25-3; Sequence=VSP_013329, VSP_013330, VSP_013331;
CC Name=4;
CC IsoId=Q86V25-4; Sequence=VSP_013332, VSP_013333;
CC Name=5;
CC IsoId=Q86V25-5; Sequence=VSP_013334;
CC Name=6;
CC IsoId=Q86V25-6; Sequence=VSP_054104;
CC -!- DEVELOPMENTAL STAGE: Expressed in various embryonic organs at 6 to 12
CC embryonic weeks. Detected in vessels from 20-week embryonic organs as
CC well as in endothelial cells from large vessels in neonate.
CC {ECO:0000269|PubMed:16528006}.
CC -!- INDUCTION: By VEGF. {ECO:0000269|PubMed:16528006}.
CC -!- SIMILARITY: Belongs to the transglutaminase-like superfamily. Vasohibin
CC family. {ECO:0000305}.
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DR EMBL; AY834202; AAX39752.1; -; mRNA.
DR EMBL; AK022567; BAB14103.1; -; mRNA.
DR EMBL; AK302675; BAG63907.1; -; mRNA.
DR EMBL; AL592449; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC028194; AAH28194.1; -; mRNA.
DR EMBL; BC051856; AAH51856.1; -; mRNA.
DR EMBL; BC053836; AAH53836.1; -; mRNA.
DR CCDS; CCDS1511.1; -. [Q86V25-5]
DR CCDS; CCDS44315.1; -. [Q86V25-2]
DR CCDS; CCDS44316.1; -. [Q86V25-6]
DR CCDS; CCDS73026.1; -. [Q86V25-1]
DR RefSeq; NP_001129946.1; NM_001136474.2. [Q86V25-2]
DR RefSeq; NP_001129947.1; NM_001136475.2. [Q86V25-6]
DR RefSeq; NP_001287985.1; NM_001301056.1. [Q86V25-1]
DR RefSeq; NP_079025.2; NM_024749.4. [Q86V25-5]
DR RefSeq; XP_011508289.1; XM_011509987.2.
DR RefSeq; XP_011508290.1; XM_011509988.2.
DR RefSeq; XP_016857840.1; XM_017002351.1.
DR PDB; 6J4O; X-ray; 2.30 A; A=46-296.
DR PDB; 6J4P; X-ray; 1.60 A; A=46-296.
DR PDB; 6J4Q; X-ray; 2.70 A; A/C/F/J=46-296.
DR PDB; 6J4S; X-ray; 2.80 A; A=1-355.
DR PDB; 6J4V; X-ray; 2.10 A; A=46-296.
DR PDB; 6QBY; X-ray; 2.09 A; A/C=40-295.
DR PDBsum; 6J4O; -.
DR PDBsum; 6J4P; -.
DR PDBsum; 6J4Q; -.
DR PDBsum; 6J4S; -.
DR PDBsum; 6J4V; -.
DR PDBsum; 6QBY; -.
DR AlphaFoldDB; Q86V25; -.
DR SMR; Q86V25; -.
DR BioGRID; 122902; 11.
DR IntAct; Q86V25; 7.
DR STRING; 9606.ENSP00000428324; -.
DR iPTMnet; Q86V25; -.
DR PhosphoSitePlus; Q86V25; -.
DR BioMuta; VASH2; -.
DR EPD; Q86V25; -.
DR jPOST; Q86V25; -.
DR MassIVE; Q86V25; -.
DR PeptideAtlas; Q86V25; -.
DR PRIDE; Q86V25; -.
DR ProteomicsDB; 5557; -.
DR ProteomicsDB; 69954; -. [Q86V25-1]
DR ProteomicsDB; 69955; -. [Q86V25-2]
DR ProteomicsDB; 69956; -. [Q86V25-3]
DR ProteomicsDB; 69957; -. [Q86V25-4]
DR ProteomicsDB; 69958; -. [Q86V25-5]
DR Antibodypedia; 47116; 152 antibodies from 22 providers.
DR DNASU; 79805; -.
DR Ensembl; ENST00000366964.7; ENSP00000355931.4; ENSG00000143494.16. [Q86V25-4]
DR Ensembl; ENST00000366965.6; ENSP00000355932.2; ENSG00000143494.16. [Q86V25-5]
DR Ensembl; ENST00000366966.6; ENSP00000430319.1; ENSG00000143494.16. [Q86V25-2]
DR Ensembl; ENST00000366967.6; ENSP00000429040.1; ENSG00000143494.16. [Q86V25-6]
DR Ensembl; ENST00000366968.8; ENSP00000355935.4; ENSG00000143494.16. [Q86V25-2]
DR Ensembl; ENST00000517399.3; ENSP00000428324.1; ENSG00000143494.16. [Q86V25-1]
DR GeneID; 79805; -.
DR KEGG; hsa:79805; -.
DR MANE-Select; ENST00000517399.3; ENSP00000428324.1; NM_001301056.2; NP_001287985.1.
DR UCSC; uc001hju.3; human. [Q86V25-1]
DR CTD; 79805; -.
DR DisGeNET; 79805; -.
DR GeneCards; VASH2; -.
DR HGNC; HGNC:25723; VASH2.
DR HPA; ENSG00000143494; Tissue enhanced (testis).
DR MIM; 610471; gene.
DR neXtProt; NX_Q86V25; -.
DR OpenTargets; ENSG00000143494; -.
DR PharmGKB; PA145147736; -.
DR VEuPathDB; HostDB:ENSG00000143494; -.
DR eggNOG; ENOG502QPPX; Eukaryota.
DR GeneTree; ENSGT00390000012703; -.
DR HOGENOM; CLU_1577966_0_0_1; -.
DR InParanoid; Q86V25; -.
DR OMA; WGHVERV; -.
DR PhylomeDB; Q86V25; -.
DR TreeFam; TF329370; -.
DR PathwayCommons; Q86V25; -.
DR Reactome; R-HSA-8955332; Carboxyterminal post-translational modifications of tubulin.
DR SignaLink; Q86V25; -.
DR BioGRID-ORCS; 79805; 12 hits in 1069 CRISPR screens.
DR GenomeRNAi; 79805; -.
DR Pharos; Q86V25; Tbio.
DR PRO; PR:Q86V25; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q86V25; protein.
DR Bgee; ENSG00000143494; Expressed in cortical plate and 114 other tissues.
DR ExpressionAtlas; Q86V25; baseline and differential.
DR Genevisible; Q86V25; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IDA:UniProtKB.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IDA:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0061564; P:axon development; IMP:UniProtKB.
DR GO; GO:0140253; P:cell-cell fusion; IDA:MGI.
DR GO; GO:0060716; P:labyrinthine layer blood vessel development; IEA:Ensembl.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IDA:MGI.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IDA:MGI.
DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR GO; GO:0045765; P:regulation of angiogenesis; IBA:GO_Central.
DR GO; GO:0000768; P:syncytium formation by plasma membrane fusion; IEA:Ensembl.
DR InterPro; IPR028131; VASH1.
DR PANTHER; PTHR15750; PTHR15750; 1.
DR Pfam; PF14822; Vasohibin; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Carboxypeptidase; Cytoplasm;
KW Cytoskeleton; Hydrolase; Phosphoprotein; Protease; Reference proteome;
KW Secreted.
FT CHAIN 1..355
FT /note="Tubulinyl-Tyr carboxypeptidase 2"
FT /id="PRO_0000189982"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 297..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 158
FT /evidence="ECO:0000269|PubMed:29146869,
FT ECO:0000305|PubMed:26794318"
FT ACT_SITE 193
FT /evidence="ECO:0000305|PubMed:26794318"
FT ACT_SITE 210
FT /evidence="ECO:0000305|PubMed:26794318"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT VAR_SEQ 1..142
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013329"
FT VAR_SEQ 1..104
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054104"
FT VAR_SEQ 1..65
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_013328"
FT VAR_SEQ 122..166
FT /note="QYNHTGTQFFEIRKMRPLSGLMETAKEMTRESLPIKCLEAVILGI -> H
FT (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013334"
FT VAR_SEQ 167..169
FT /note="YLT -> THS (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013332"
FT VAR_SEQ 170..355
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013333"
FT VAR_SEQ 294..298
FT /note="ILKPA -> GLCSH (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013330"
FT VAR_SEQ 299..355
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013331"
FT MUTAGEN 63..67
FT /note="WERMW->EERME: Disrupted interaction with SVBP.
FT Reduced tyrosine carboxypeptidase activity."
FT /evidence="ECO:0000269|PubMed:31235911"
FT MUTAGEN 123
FT /note="Y->A: Reduced tyrosine carboxypeptidase activity."
FT /evidence="ECO:0000269|PubMed:31235911"
FT MUTAGEN 134
FT /note="R->A: Slightly reduced tyrosine carboxypeptidase
FT activity."
FT /evidence="ECO:0000269|PubMed:31235911"
FT MUTAGEN 135
FT /note="K->A: Reduced tyrosine carboxypeptidase activity."
FT /evidence="ECO:0000269|PubMed:31235911"
FT MUTAGEN 154..155
FT /note="LP->EE: Disrupted interaction with SVBP. Reduced
FT tyrosine carboxypeptidase activity."
FT /evidence="ECO:0000269|PubMed:31235911"
FT MUTAGEN 157
FT /note="K->A: Reduced tyrosine carboxypeptidase activity."
FT /evidence="ECO:0000269|PubMed:31235911"
FT MUTAGEN 158
FT /note="C->A: Abolished tyrosine carboxypeptidase activity.
FT No effect on binding to microtubule."
FT /evidence="ECO:0000269|PubMed:29146869,
FT ECO:0000269|PubMed:31235911"
FT MUTAGEN 192
FT /note="H->A: No effect on tyrosine carboxypeptidase
FT activity."
FT /evidence="ECO:0000269|PubMed:31235911"
FT MUTAGEN 193
FT /note="H->A: Strongly reduced tyrosine carboxypeptidase
FT activity."
FT /evidence="ECO:0000269|PubMed:31235911"
FT MUTAGEN 210
FT /note="S->A: Reduced tyrosine carboxypeptidase activity."
FT /evidence="ECO:0000269|PubMed:31235911"
FT MUTAGEN 211
FT /note="R->A,H: Reduced tyrosine carboxypeptidase activity."
FT /evidence="ECO:0000269|PubMed:31235911"
FT MUTAGEN 215
FT /note="L->A: Slightly reduced tyrosine carboxypeptidase
FT activity."
FT /evidence="ECO:0000269|PubMed:31235911"
FT HELIX 60..73
FT /evidence="ECO:0007829|PDB:6J4P"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:6J4S"
FT HELIX 77..85
FT /evidence="ECO:0007829|PDB:6J4P"
FT HELIX 107..121
FT /evidence="ECO:0007829|PDB:6J4P"
FT STRAND 126..131
FT /evidence="ECO:0007829|PDB:6J4P"
FT HELIX 139..152
FT /evidence="ECO:0007829|PDB:6J4P"
FT HELIX 158..169
FT /evidence="ECO:0007829|PDB:6J4P"
FT STRAND 175..186
FT /evidence="ECO:0007829|PDB:6J4P"
FT STRAND 189..200
FT /evidence="ECO:0007829|PDB:6J4P"
FT STRAND 203..207
FT /evidence="ECO:0007829|PDB:6J4P"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:6J4P"
FT STRAND 218..224
FT /evidence="ECO:0007829|PDB:6J4P"
FT HELIX 225..238
FT /evidence="ECO:0007829|PDB:6J4P"
FT STRAND 242..248
FT /evidence="ECO:0007829|PDB:6J4P"
FT STRAND 266..270
FT /evidence="ECO:0007829|PDB:6J4P"
FT TURN 271..273
FT /evidence="ECO:0007829|PDB:6QBY"
FT HELIX 276..292
FT /evidence="ECO:0007829|PDB:6J4P"
SQ SEQUENCE 355 AA; 40450 MW; C74C313FEF6A0837 CRC64;
MTGSAADTHR CPHPKGAKGT RSRSSHARPV SLATSGGSEE EDKDGGVLFH VNKSGFPIDS
HTWERMWMHV AKVHPKGGEM VGAIRNAAFL AKPSIPQVPN YRLSMTIPDW LQAIQNYMKT
LQYNHTGTQF FEIRKMRPLS GLMETAKEMT RESLPIKCLE AVILGIYLTN GQPSIERFPI
SFKTYFSGNY FHHVVLGIYC NGRYGSLGMS RRAELMDKPL TFRTLSDLIF DFEDSYKKYL
HTVKKVKIGL YVPHEPHSFQ PIEWKQLVLN VSKMLRADIR KELEKYARDM RMKILKPASA
HSPTQVRSRG KSLSPRRRQA SPPRRLGRRE KSPALPEKKV ADLSTLNEVG YQIRI
